0194452 - UOCHB-X 20020120 RIV GB eng J - Journal Article
Horn, Martin - Baudyš, M. - Voburka, Zdeněk - Kluh, Ivan - Vondrášek, Jiří - Mareš, Michael
Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).
Protein Science. Roč. 11, - (2002), s. 933-943. ISSN 0961-8368. E-ISSN 1469-896X
R&D Projects: GA AV ČR IAA4055006; GA ČR GA522/00/1553; GA MŠMT LN00A032; GA ČR GP203/01/D008
Institutional research plan: CEZ:AV0Z4055905
Keywords : cathepsin C * cysteine protease
Subject RIV: CE - Biochemistry
Impact factor: 3.546, year: 2002

The mature bovine cathepsin C (CC) molecule is composed of four identical monomers, each proteolytically processed into three chains. Five intrachain disulfides and three nonpaired cysteine residues per monomer were identified. Beside catalytic Cys234 in the active site, free-thiol Cys331 and Cys424 were characterized.
Permanent Link: http://hdl.handle.net/11104/0090127